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Penaeidin-3a (P3-a) (Pen-3a)

 PEN3A_LITVA             Reviewed;          82 AA.
P81058;
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
15-JUL-1998, sequence version 1.
20-JUN-2018, entry version 81.
RecName: Full=Penaeidin-3a;
Short=P3-a;
Short=Pen-3a;
Flags: Precursor;
Litopenaeus vannamei (Whiteleg shrimp) (Penaeus vannamei).
Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Crustacea; Multicrustacea;
Malacostraca; Eumalacostraca; Eucarida; Decapoda; Dendrobranchiata;
Penaeoidea; Penaeidae; Litopenaeus.
NCBI_TaxID=6689;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-81, PYROGLUTAMATE
FORMATION AT GLN-20, FUNCTION, MASS SPECTROMETRY, AND AMIDATION AT
SER-81.
TISSUE=Hemocyte;
PubMed=9353298; DOI=10.1074/jbc.272.45.28398;
Destoumieux D., Bulet P., Loew D., van Dorsselaer A., Rodriguez J.,
Bachere E.;
"Penaeidins, a new family of antimicrobial peptides isolated from the
shrimp Penaeus vannamei (Decapoda).";
J. Biol. Chem. 272:28398-28406(1997).
[2]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=12242595; DOI=10.1007/s00251-002-0487-z;
Cuthbertson B.J., Shepard E.F., Chapman R.W., Gross P.S.;
"Diversity of the penaeidin antimicrobial peptides in two shrimp
species.";
Immunogenetics 54:442-445(2002).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 20-82, PROTEIN SEQUENCE OF 20-31, AND
FUNCTION.
PubMed=10561573; DOI=10.1046/j.1432-1327.1999.00855.x;
Destoumieux D., Bulet P., Strub J.-M., van Dorsselaer A., Bachere E.;
"Recombinant expression and range of activity of penaeidins,
antimicrobial peptides from penaeid shrimp.";
Eur. J. Biochem. 266:335-346(1999).
[4]
CHITIN-BINDING PROPERTIES, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
AND DEVELOPMENTAL STAGE.
TISSUE=Hemocyte;
PubMed=10639333;
Destoumieux D., Munoz M., Cosseau C., Rodriguez J., Bulet P.,
Comps M., Bachere E.;
"Penaeidins, antimicrobial peptides with chitin-binding activity, are
produced and stored in shrimp granulocytes and released after
microbial challenge.";
J. Cell Sci. 113:461-469(2000).
[5]
REVIEW.
PubMed=11028917; DOI=10.1007/PL00000764;
Destoumieux D., Munoz M., Bulet P., Bachere E.;
"Penaeidins, a family of antimicrobial peptides from penaeid shrimp
(Crustacea, Decapoda).";
Cell. Mol. Life Sci. 57:1260-1271(2000).
[6]
STRUCTURE BY NMR, AND DISULFIDE BONDS.
PubMed=12842879; DOI=10.1074/jbc.M305450200;
Yang Y., Poncet J., Garnier J., Zatylny C., Bachere E., Aumelas A.;
"Solution structure of the recombinant penaeidin-3, a shrimp
antimicrobial peptide.";
J. Biol. Chem. 278:36859-36867(2003).
-!- FUNCTION: Antibacterial activity against M.luteus and E.coli
bacteria. Antifungal activity against N.crassa and F.oxysporum.
Presents chitin-binding activity. {ECO:0000269|PubMed:10561573,
ECO:0000269|PubMed:9353298}.
-!- SUBCELLULAR LOCATION: Cytoplasmic granule
{ECO:0000269|PubMed:10639333}. Note=Cytoplasmic granules of
hemocytes and to a lesser extent in small granules of hemocytes.
-!- TISSUE SPECIFICITY: Higher expression in hemocytes and to a lesser
extent in heart, testis, gills, intestine, lymphoid organ and
hepatopancreas. Traces in eyes and subcuticular epithelium. Not
present in the brain. {ECO:0000269|PubMed:10639333}.
-!- DEVELOPMENTAL STAGE: Expression decreases 3 hours after microbial
challenge to return to control levels after 12 hours and slightly
increases after 24 hours. {ECO:0000269|PubMed:10639333}.
-!- PTM: The N-terminus forms pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:9353298}.
-!- MASS SPECTROMETRY: Mass=6617.4; Method=MALDI; Range=20-81;
Evidence={ECO:0000269|PubMed:9353298};
-!- SIMILARITY: Belongs to the penaeidin family. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; Y14926; CAA75143.1; -; mRNA.
EMBL; AF387661; AAK73084.1; -; mRNA.
EMBL; AF387662; AAK73085.1; -; mRNA.
EMBL; AF387663; AAK73086.1; -; mRNA.
EMBL; AF390139; AAK77532.1; -; mRNA.
PDB; 1UEO; NMR; -; A=20-82.
PDBsum; 1UEO; -.
ProteinModelPortal; P81058; -.
SMR; P81058; -.
EvolutionaryTrace; P81058; -.
GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
GO; GO:0008061; F:chitin binding; IDA:UniProtKB.
GO; GO:0042742; P:defense response to bacterium; IDA:UniProtKB.
GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IMP:CAFA.
GO; GO:0031640; P:killing of cells of other organism; IEA:UniProtKB-KW.
InterPro; IPR009226; Penaeidin.
Pfam; PF05927; Penaeidin; 1.
1: Evidence at protein level;
3D-structure; Amidation; Antibiotic; Antimicrobial; Chitin-binding;
Direct protein sequencing; Disulfide bond; Fungicide;
Pyrrolidone carboxylic acid; Signal.
SIGNAL 1 19 {ECO:0000269|PubMed:10561573,
ECO:0000269|PubMed:9353298}.
CHAIN 20 81 Penaeidin-3a.
/FTId=PRO_0000023506.
COMPBIAS 29 47 Pro-rich.
MOD_RES 20 20 Pyrrolidone carboxylic acid.
{ECO:0000269|PubMed:9353298}.
MOD_RES 81 81 Serine amide.
{ECO:0000269|PubMed:9353298}.
DISULFID 51 66 {ECO:0000269|PubMed:12842879}.
DISULFID 55 73 {ECO:0000269|PubMed:12842879}.
DISULFID 67 74 {ECO:0000269|PubMed:12842879}.
STRAND 26 30 {ECO:0000244|PDB:1UEO}.
HELIX 60 70 {ECO:0000244|PDB:1UEO}.
SEQUENCE 82 AA; 8748 MW; E60E09BB305521FD CRC64;
MRLVVCLVFL ASFALVCQGQ VYKGGYTRPI PRPPPFVRPL PGGPIGPYNG CPVSCRGISF
SQARSCCSRL GRCCHVGKGY SG


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